Structural highlights
Function
[RNS_BOVIN] This enzyme hydrolyzes both single- and double-stranded RNA.
Publication Abstract from PubMed
Bovine seminal ribonuclease (BS-RNase) acquires an interesting anti-tumor activity associated with the swapping on the N-termini. The first direct experimental evidence on the formation of a C-terminal swapped dimer (C-dimer) obtained from the monomeric derivative of BS-RNase, although under non-native conditions, is here reported. The X-ray model of this dimer reveals a quaternary structure different from that of the C-dimer of RNase A, due to the presence of three mutations in the hinge peptide 111-116. The mutations increase the hinge peptide flexibility and decrease the stability of the C-dimer against dissociation. The biological implications of the structural data are also discussed.
The multiple forms of Bovine Seminal Ribonuclease: structure and stability of a C-terminal swapped dimer.,Sica F, Pica A, Merlino A, Krauss IR, Ercole C, Picone D FEBS Lett. 2013 Oct 15. pii: S0014-5793(13)00745-X. doi:, 10.1016/j.febslet.2013.10.003. PMID:24140346[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sica F, Pica A, Merlino A, Krauss IR, Ercole C, Picone D. The multiple forms of Bovine Seminal Ribonuclease: structure and stability of a C-terminal swapped dimer. FEBS Lett. 2013 Oct 15. pii: S0014-5793(13)00745-X. doi:, 10.1016/j.febslet.2013.10.003. PMID:24140346 doi:http://dx.doi.org/10.1016/j.febslet.2013.10.003
